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Characterization and molecular cloning of thermostable alpha-amylase fromStreptomycessp.To1

โœ Scribed by Lotfi Mellouli; Raoudha Ghorbel; Alya Kammoun; Monia Mezghani; Samir Bejar


Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
353 KB
Volume
18
Category
Article
ISSN
0141-5492

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โœฆ Synopsis


A new thermophilic Streptomyces sp. TO1, isolated from Tunisian soil, produced a thermostable alpha-amylase and pullulanase. The gene encoding for the alpha-amylase activity was cloned into the multicopy cloning plasmid pLM1 using S. lividans ZX1 as host strain. The ZX1 / pLM1 strain has the same activity than the initial TO1 strain and about 25 fold higher activity than the ZX1 strain. This alpha-amylase has an optimum of pH and temperature at 6 and 700C respectively.


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